Protein information for: OR52E2



MFLPNDTQFHPSSFLLLGIPGLETLHIWIGFPFCAVYMIALIGNFTILLV
IKTDSSLHQPMFYFLAMLATTDVGLSTATIPKMLGIFWINLRGIIFEACL
TQMFFIHNFTLMESAVLVAMAYDSYVAICNPLQYSAILTNKVVSVIGLGV
FVRALIFVIPSILLILRLPFCGNHVIPHTYCEHMGLAHLSCASIKINIIY
GLCAICNLVFDITVIALSYVHILCAVFRLPTHEARLKSLSTCGSHVCVIL
AFYTPALFSFMTHRFGRNVPRYIHILLANLYVVVPPMLNPVIYGVRTKQI
YKCVKKILLQEQGMEKEEYLIHTRF
In red: predicted N-glycosylation site.
In magenta: Conserved cysteines that are predicted to form a disulfide bond.
Underlined and bold: TM regions.

Predicted binding site residues (CDRs) are highlighted according to the following amino acid color code:
| | basic (H,R,K)
| | hydrophilic, no charge (Q,N,T,S)
| | aliphatic (M,A,I,L,V)
| | aromatic (F,Y,W)
| | helix breakers (G,P)
| | acidic (D,E)
| | cysteine (C)

Sequences of the TM regions:

TM

Start position

End position

Sequence

TM1 26 52 HIWIGFPFCAVYMIALIGNFTILLVIK
TM2 63 85 YFLAMLATTDVGLSTATIPKMLG
TM3 100 120 LTQMFFIHNFTLMESAVLVAM
TM4 143 163 VSVIGLGVFVRALIFVIPSIL
TM5 200 220 YGLCAICNLVFDITVIALSYV
TM6 242 266 CGSHVCVILAFYTPALFSFMTHRFG
TM7 274 293 HILLANLYVVVPPMLNPVIY

The information was derived from a multiple alignment of ORs, based on the algorithms of Man et al. Protein Sci. 2004 Jan;13(1):240-54.
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